A study of the kinetics of the reaction between ferrocene monocarboxylic acid and glucose oxidase using the rotating-disc electrode

• Published in: Journal of electroanalytical chemistry (Lausanne, Switzerland) Vol. 397; no. 1; pp. 53 - 60
• Main Authors: Bartlett, P.N., Pratt, K.F.E.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.11.1995; Elsevier Science
• Subjects: Amperometric biosensors; Biological and medical sciences; Biosensors; Biotechnology; Chemistry; Electrochemistry; Exact sciences and technology; Ferrocene monocarboxylic acid; Fundamental and applied biological sciences. Psychology; General and physical chemistry; Glucose oxidase; Kinetics and mechanism of reactions; Methods. Procedures. Technologies; Reaction kinetics; Rotating-disc electrode; Various methods and equipments; Glucose oxidase; Amperometric biosensors; Ferrocene monocarboxylic acid; Rotating-disc electrode; Reaction kinetics; Phosphates; Aldose; Enzyme; Rotating disk electrode; Glucose; Experimental study; Buffer solution; Carbon; Metallocene; Operating conditions; Iron Organic compounds; Carboxylic acid; Medium effect; Biosensor; Amperometry; Reaction mechanism; Oxidoreductases; Kinetics; Electrochemical reaction; Glassy state; Enzymatic reaction
• ISSN: 1572-6657; 1873-2569
• DOI: 10.1016/0022-0728(95)04173-8

In this paper we present the result of a study of the glucose|glucose oxidase|ferrocene monocarboxylic acid system using the rotating-disc electrode. The results of experiments carried out over a wide range of experimental conditions (rotation speed, enzyme, mediator and substrate concentration) are compared with the theoretical model presented by Albery et al. ( J. Electroanal. Chem., 323 (1992) 77). Good agreement between the experiments and theory is demonstrated for most of the available range of experimental conditions, and the method is shown to be a good one for the determination of the rate of reaction of the enzyme and mediator. In the case where the enzyme substrate kinetics are rate limiting it is shown that the correct interpretation of the data is more difficult because of the effects of concentration polarization of the substrate. An approach to overcoming this problem is described. The experimental techniques and analysis described in this paper should be generally applicable to studies of the homogeneous kinetics of mediated enzyme reactions.